David D Boehr

Summary

Affiliation: Pennsylvania State University
Country: USA

Publications

  1. pmc Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance
    Xiaorong Yang
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Biochemistry 49:9361-71. 2010
  2. doi request reprint Promiscuity in protein-RNA interactions: conformational ensembles facilitate molecular recognition in the spliceosome: conformational diversity in U2AF⁶⁵ facilitates binding to diverse RNA sequences
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, 240 Chemistry Building, University Park, PA, USA
    Bioessays 34:174-80. 2012
  3. pmc The role of dynamic conformational ensembles in biomolecular recognition
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, USA
    Nat Chem Biol 5:789-96. 2009
  4. pmc Motif D of viral RNA-dependent RNA polymerases determines efficiency and fidelity of nucleotide addition
    Xiaorong Yang
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Structure 20:1519-27. 2012
  5. doi request reprint Long-range interactions in the α subunit of tryptophan synthase help to coordinate ligand binding, catalysis, and substrate channeling
    Jennifer M Axe
    Department of Chemistry, Pennsylvania State University, 240 Chemistry Building, University Park, PA 16802, USA
    J Mol Biol 425:1527-45. 2013
  6. doi request reprint Differences in the catalytic mechanisms of mesophilic and thermophilic indole-3-glycerol phosphate synthase enzymes at their adaptive temperatures
    Margot J Zaccardi
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Biochem Biophys Res Commun 418:324-9. 2012
  7. pmc Functional Identification of the General Acid and Base in the Dehydration Step of Indole-3-glycerol Phosphate Synthase Catalysis
    Margot J Zaccardi
    From the Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802
    J Biol Chem 288:26350-6. 2013
  8. doi request reprint During transitions proteins make fleeting bonds
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Cell 139:1049-51. 2009

Collaborators

Detail Information

Publications8

  1. pmc Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance
    Xiaorong Yang
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Biochemistry 49:9361-71. 2010
    ..Mutation of Gly64 results in structural and/or dynamic changes to the network that may affect polymerase fidelity...
  2. doi request reprint Promiscuity in protein-RNA interactions: conformational ensembles facilitate molecular recognition in the spliceosome: conformational diversity in U2AF⁶⁵ facilitates binding to diverse RNA sequences
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, 240 Chemistry Building, University Park, PA, USA
    Bioessays 34:174-80. 2012
    ..Similar binding pathways in other systems have important consequences in biological regulation, molecular evolution, and information storage...
  3. pmc The role of dynamic conformational ensembles in biomolecular recognition
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, USA
    Nat Chem Biol 5:789-96. 2009
    ....
  4. pmc Motif D of viral RNA-dependent RNA polymerases determines efficiency and fidelity of nucleotide addition
    Xiaorong Yang
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Structure 20:1519-27. 2012
    ..We conclude that motif D of RdRps and, by inference, RTs is the functional equivalent to the fidelity helix of other polymerases...
  5. doi request reprint Long-range interactions in the α subunit of tryptophan synthase help to coordinate ligand binding, catalysis, and substrate channeling
    Jennifer M Axe
    Department of Chemistry, Pennsylvania State University, 240 Chemistry Building, University Park, PA 16802, USA
    J Mol Biol 425:1527-45. 2013
    ..During catalytic turnover, the protein becomes more rigid on the millisecond timescale and the active-site dynamics are driven to a faster nanosecond timescale...
  6. doi request reprint Differences in the catalytic mechanisms of mesophilic and thermophilic indole-3-glycerol phosphate synthase enzymes at their adaptive temperatures
    Margot J Zaccardi
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Biochem Biophys Res Commun 418:324-9. 2012
    ....
  7. pmc Functional Identification of the General Acid and Base in the Dehydration Step of Indole-3-glycerol Phosphate Synthase Catalysis
    Margot J Zaccardi
    From the Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802
    J Biol Chem 288:26350-6. 2013
    ....
  8. doi request reprint During transitions proteins make fleeting bonds
    David D Boehr
    Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
    Cell 139:1049-51. 2009
    ..2009) show that transient hydrogen bonds are critical to the conformational transition of the nitrogen regulatory protein NtrC between its native state and its active state...